Proteolytic degradation of heat shock protein A2 occurs in response to oxidative stress in male germ cells of the mouse

The present study investigated the effects of ferulic acid (FA) on pentylenetetrazole (PTZ)-induced seizures, oxidative stress markers (malondialdehyde (MDA), catalase, and reduced glutathione (GSH)), connexin (Cx) 43, heat shock protein 70 (Hsp 70), and monoamines (serotonin (5-HT) and norepinephrine (NE)) levels in a rat model of PTZ-induced kindling. Sixty Sprague Dawley rats were divided into 5 equal groups: (a) normal group; (b) FA group: normal rats received FA at a dose of 40 mg/kg daily; (c) PTZ group: normal rats received PTZ at a dose of 50 mg/kg i.p. on alternate days for 15 days; (d) FA-before group: treatment was the same as for the PTZ group, except rats received FA; and (e) FA-after group: rats received FA from sixth dose of PTZ. PTZ caused a significant increase in MDA, Cx43, and Hsp70 along with a significant decrease in GSH, 5-HT, and NE levels and CAT activity in the hippocampus (p < 0.05). Pre- and post-treatment with FA caused significant improvement in behavioral parameters, MDA, CAT, GSH, 5-HT, NE, Cx43 expression, and Hsp70 expression in the hippocampal region (p < 0.05). We conclude that FA has neuroprotective effects in PTZ-induced epilepsy, which might be due to attenuation of oxidative stress and Cx43 expression and upregulation of neuroprotective Hsp70 and neurotransmitters (5-HT and NE).

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The chloroplast small heat shock protein undergoes oxidation-dependent conformational changes and may protect plants from oxidative stress

Cell Stress and Chaperones ◽

10.1379/1466-1268(1999)004<0129:tcshsp>2.3.co;2 ◽

1999 ◽

Vol 4 (2) ◽

pp. 129 ◽

Cited By ~ 88

Author(s):

Ulrika Härndahl ◽

Roberta Buffoni Hall ◽

Katherine W. Osteryoung ◽

Elizabeth Vierling ◽

Janet F. Bornman ◽

...

Keyword(s):

Oxidative Stress ◽

Heat Shock ◽

Heat Shock Protein ◽

Conformational Changes ◽

Small Heat Shock Protein

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Exercise protects against doxorubicin-induced oxidative stress and proteolysis in skeletal muscle

Journal of Applied Physiology ◽

10.1152/japplphysiol.00677.2010 ◽

2011 ◽

Vol 110 (4) ◽

pp. 935-942 ◽

Cited By ~ 69

Author(s):

Ashley J. Smuder ◽

Andreas N. Kavazis ◽

Kisuk Min ◽

Scott K. Powers

Keyword(s):

Oxidative Stress ◽

Skeletal Muscle ◽

Antioxidant Enzymes ◽

Heat Shock ◽

Heat Shock Protein ◽

Oxidative Damage ◽

Muscle Fibers ◽

Muscular Exercise ◽

Protease Activation ◽

Exercise Induced

Doxorubicin (Dox) is a potent antitumor agent used in cancer treatment. Unfortunately, Dox is myotoxic and results in significant reductions in skeletal muscle mass and function. Complete knowledge of the mechanism(s) by which Dox induces toxicity in skeletal muscle is incomplete, but it is established that Dox-induced toxicity is associated with increased generation of reactive oxygen species and oxidative damage within muscle fibers. Since muscular exercise promotes the expression of numerous cytoprotective proteins (e.g., antioxidant enzymes, heat shock protein 72), we hypothesized that muscular exercise will attenuate Dox-induced damage in exercise-trained muscle fibers. To test this postulate, Sprague-Dawley rats were randomly assigned to the following groups: sedentary, exercise, sedentary with Dox, or exercise with Dox. Our results show increased oxidative stress and activation of cellular proteases (calpain and caspase-3) in skeletal muscle of animals treated with Dox. Importantly, our findings reveal that exercise can prevent the Dox-induced oxidative damage and protease activation in the trained muscle. This exercise-induced protection against Dox-induced toxicity may be due, at least in part, to an exercise-induced increase in muscle levels of antioxidant enzymes and heat shock protein 72. Together, these novel results demonstrate that muscular exercise is a useful countermeasure that can protect skeletal muscle against Dox treatment-induced oxidative stress and protease activation in skeletal muscles.

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